4xae
Structure of Feruloyl-CoA 6-hydroxylase (F6H) from Arabidopsis thaliana
Structural highlights
FunctionF6H1_ARATH 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD)involved in scopoletin biosynthesis. Converts feruloyl CoA into 6'-hydroxyferuloyl CoA but has no activity with ferulic acid, feruloylquinic acid, caffeic acid, caffeoyl CoA, p-coumaric acid, cinnamic acid, cinnamoyl CoA or benzoyl CoA.[1] Publication Abstract from PubMedCoumarins belong to an important class of plant secondary metabolites. Feruloyl-CoA 6'-hydroxylase (F6'H), a 2-oxoglutarate dependent dioxygenase (2OGD), catalyzes a pivotal step in the biosynthesis of a simple coumarin scopoletin. In this study, we determined the 3-dimensional structure of the F6'H1 apo enzyme by X-ray crystallography. It is the first reported structure of a 2OGD enzyme involved in coumarin biosynthesis and closely resembles the structure of Arabidopsis thaliana anthocyanidin synthase. To better understand the mechanism of enzyme catalysis and substrate specificity, we also generated a homology model of a related ortho-hydroxylase (C2'H) from sweet potato. By comparing these two structures, we targeted two amino acid residues and verified their roles in substrate binding and specificity by site-directed mutagenesis. Structural Insights into Substrate Specificity of Feruloyl-CoA 6'-Hydroxylase from Arabidopsis thaliana.,Sun X, Zhou D, Kandavelu P, Zhang H, Yuan Q, Wang BC, Rose J, Yan Y Sci Rep. 2015 May 20;5:10355. doi: 10.1038/srep10355. PMID:25993561[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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